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Impact of heterologous expression of Escherichia coli UDP-glucose pyrophosphorylase on trehalose and glycogen synthesis in Corynebacterium glutamicum.
Appl Environ Microbiol 2004; 70(7):3845-54AE

Abstract

Trehalose is a disaccharide with a wide range of applications in the food industry. We recently proposed a strategy for trehalose production based on improved strains of the gram-positive bacterium Corynebacterium glutamicum. This microorganism synthesizes trehalose through two major pathways, OtsBA and TreYZ, by using UDP-glucose and ADP-glucose, respectively, as the glucosyl donors. In this paper we describe improvement of the UDP-glucose supply through heterologous expression in C. glutamicum of the UDP-glucose pyrophosphorylase gene from Escherichia coli, either expressed alone or coexpressed with the E. coli ots genes (galU otsBA synthetic operon). The impact of such expression on trehalose accumulation and excretion, glycogen accumulation, and the growth pattern of new recombinant strains is described. Expression of the galU otsBA synthetic operon resulted in a sixfold increase in the accumulated and excreted trehalose relative to that in a wild-type strain. Surprisingly, single expression of galU also resulted in an increase in the accumulated trehalose. This increase in trehalose synthesis was abolished upon deletion of the TreYZ pathway. These results proved that UDP-glucose has an important role not only in the OtsBA pathway but also in the TreYZ pathway.

Authors+Show Affiliations

Departmento de Ingeniería y Bioprocesos, Escuela de Ingeniería, Pontificia Universidad Católica de Chile, Casilla 306 Correo 22, Santiago, Chile.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15240254

Citation

Padilla, Leandro, et al. "Impact of Heterologous Expression of Escherichia Coli UDP-glucose Pyrophosphorylase On Trehalose and Glycogen Synthesis in Corynebacterium Glutamicum." Applied and Environmental Microbiology, vol. 70, no. 7, 2004, pp. 3845-54.
Padilla L, Morbach S, Krämer R, et al. Impact of heterologous expression of Escherichia coli UDP-glucose pyrophosphorylase on trehalose and glycogen synthesis in Corynebacterium glutamicum. Appl Environ Microbiol. 2004;70(7):3845-54.
Padilla, L., Morbach, S., Krämer, R., & Agosin, E. (2004). Impact of heterologous expression of Escherichia coli UDP-glucose pyrophosphorylase on trehalose and glycogen synthesis in Corynebacterium glutamicum. Applied and Environmental Microbiology, 70(7), pp. 3845-54.
Padilla L, et al. Impact of Heterologous Expression of Escherichia Coli UDP-glucose Pyrophosphorylase On Trehalose and Glycogen Synthesis in Corynebacterium Glutamicum. Appl Environ Microbiol. 2004;70(7):3845-54. PubMed PMID: 15240254.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Impact of heterologous expression of Escherichia coli UDP-glucose pyrophosphorylase on trehalose and glycogen synthesis in Corynebacterium glutamicum. AU - Padilla,Leandro, AU - Morbach,Susanne, AU - Krämer,Reinhard, AU - Agosin,Eduardo, PY - 2004/7/9/pubmed PY - 2004/9/17/medline PY - 2004/7/9/entrez SP - 3845 EP - 54 JF - Applied and environmental microbiology JO - Appl. Environ. Microbiol. VL - 70 IS - 7 N2 - Trehalose is a disaccharide with a wide range of applications in the food industry. We recently proposed a strategy for trehalose production based on improved strains of the gram-positive bacterium Corynebacterium glutamicum. This microorganism synthesizes trehalose through two major pathways, OtsBA and TreYZ, by using UDP-glucose and ADP-glucose, respectively, as the glucosyl donors. In this paper we describe improvement of the UDP-glucose supply through heterologous expression in C. glutamicum of the UDP-glucose pyrophosphorylase gene from Escherichia coli, either expressed alone or coexpressed with the E. coli ots genes (galU otsBA synthetic operon). The impact of such expression on trehalose accumulation and excretion, glycogen accumulation, and the growth pattern of new recombinant strains is described. Expression of the galU otsBA synthetic operon resulted in a sixfold increase in the accumulated and excreted trehalose relative to that in a wild-type strain. Surprisingly, single expression of galU also resulted in an increase in the accumulated trehalose. This increase in trehalose synthesis was abolished upon deletion of the TreYZ pathway. These results proved that UDP-glucose has an important role not only in the OtsBA pathway but also in the TreYZ pathway. SN - 0099-2240 UR - https://www.unboundmedicine.com/medline/citation/15240254/Impact_of_heterologous_expression_of_Escherichia_coli_UDP_glucose_pyrophosphorylase_on_trehalose_and_glycogen_synthesis_in_Corynebacterium_glutamicum_ L2 - http://aem.asm.org/cgi/pmidlookup?view=long&pmid=15240254 DB - PRIME DP - Unbound Medicine ER -